Cation-conducting protein channels are ubiquitous regulators in biology. They locate in the phospholipid bilayer membrane of the cell and permit the passage of cations, anions, water, and other species through the barrier. Channels may be switched on or off in a process called "gating" that is well known but poorly understood. Indeed, much of the fundamental chemistry of channels is inadequately understood precisely because channels are typically large and complex proteins. Amino acid sequences for channel proteins have been known for some time but the first crystal structure of a channel protein appeared only in 1998. Our efforts have led to a family of compounds that insert in bilayer membranes and transport cations at a rate competitive with protein some channels. The significance of this effort is that the synthetic channel is modular and simple. Because of this, we may isolate functions and probe chemical issues directly within the bilayer. These simplified structures have molecular weights of less than or equal to 2000 Da but accomplish some of the functions of natural protein channels having much higher molecular weights and structural complexities. Ultimately, we hope to elaborate these relatively simple structures into drug candidates. We do not believe that elaboration of these novel structures into potential drug candidates is imminent at this early stage. It is, however, an important long-range goal of this project.